Abstract: Human prostatic acid phosphatase (PAcP) is a 100 kDa glycoprotein composed of two subunits. Recent advances demonstrate that cellular PAcP (cPAcP) functions as a protein tyrosine phosphatase by dephosphorylating ErbB-2/Neu/HER-2 at the phosphotyrosine residues in prostate cancer (PCa) cells, which results in reduced tumorigenicity. Further, the interaction of cPAcP and ErbB-2 regulates androgen sensitivity of PCa cells. Knockdown of cPAcP expression allows androgen-sensitive PCa cells to develop the castration-resistant phenotype, where cells proliferate under an androgen-reduced condition. Thus, cPAcP has a significant influence on PCa cell growth. Interestingly, promoter analysis suggests that PAcP expression can be regulated by NF-κB, via a novel binding sequence in an androgen-independent manner. Further understanding of PAcP function and regulation of expression will have a significant impact on understanding PCa progression and therapy.
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Muniyan, S.; Chaturvedi, N.K.; Dwyer, J.G.; LaGrange, C.A.; Chaney, W.G.; Lin, M.-F. Human Prostatic Acid Phosphatase: Structure, Function and Regulation. Int. J. Mol. Sci. 2013, 14, 10438-10464.
Muniyan S, Chaturvedi NK, Dwyer JG, LaGrange CA, Chaney WG, Lin M-F. Human Prostatic Acid Phosphatase: Structure, Function and Regulation. International Journal of Molecular Sciences. 2013; 14(5):10438-10464.
Muniyan, Sakthivel; Chaturvedi, Nagendra K.; Dwyer, Jennifer G.; LaGrange, Chad A.; Chaney, William G.; Lin, Ming-Fong. 2013. "Human Prostatic Acid Phosphatase: Structure, Function and Regulation." Int. J. Mol. Sci. 14, no. 5: 10438-10464.